› 4fba

X-ray diffraction
1.85Å resolution

Structure of mutant RIP from barley seeds in complex with adenine

Released:
DOI: 10.2210/pdb4fba/pdb
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Source organism: Hordeum vulgare
Primary publication:
Structures of the ribosome-inactivating protein from barley seeds reveal a unique activation mechanism.
Lee BG, Kim MK, Kim BW, Suh SW, Song HK
Acta Crystallogr D Biol Crystallogr 68 1488-500 (2012)
PMID: 23090398

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein synthesis inhibitor I Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 282 amino acids
Theoretical weight: 29.85 KDa
Source organism: Hordeum vulgare
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22244 (Residues: 2-281; Coverage: 100%)
Gene name: RIP30
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADE 4 x ADE
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2
Unit cell:
a: 130.968Å b: 142.412Å c: 84.751Å
α: 90° β: 127.52° γ: 90°
R-values:
R R work R free
0.172 0.171 0.202
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Biological activities of ribosome-inactivating proteins and their possible applications as antimicrobial, anticancer, and anti-pest agents and in neuroscience research.
Akkouh et al. (2015)
1 more

1 mention without citation

Two-substrate enzyme engineering using small libraries that combine the substrate preferences from two different variant lineages.
Mukhopadhyay et al. (2024)

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